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A0876
N-Acetyl-D-Leucin
≥99% (TLC), suitable for ligand binding assays and cell cutlure
Synonym(e):
N-acetyl-D-Leucine
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About This Item
Empirische Formel (Hill-System):
C8H15NO3
CAS-Nummer:
Molekulargewicht:
173.21
MDL-Nummer:
UNSPSC-Code:
12352209
PubChem Substanz-ID:
NACRES:
NA.26
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Produktbezeichnung
N-Acetyl-D-Leucin,
Assay
≥99% (TLC)
Qualitätsniveau
Form
powder
Methode(n)
cell culture | mammalian: suitable
ligand binding assay: suitable
Farbe
white
Lagertemp.
−20°C
SMILES String
CC(C)C[C@@H](NC(C)=O)C(O)=O
InChI
1S/C8H15NO3/c1-5(2)4-7(8(11)12)9-6(3)10/h5,7H,4H2,1-3H3,(H,9,10)(H,11,12)/t7-/m1/s1
InChIKey
WXNXCEHXYPACJF-SSDOTTSWSA-N
Anwendung
N-Acetyl-D-leucine may be used with other D-aminoacylated amino acids as a substrate for the identification, differentiation and characterization of D-aminoacylase(s)/amidohydrolase(s).
Biochem./physiol. Wirkung
N-Acetyl-D-leucine is a substrate for D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6. N-Acetyl-D-leucine is used to help differentiate members of the amidohydrolase enzyme superfamily. It is a preferred substrate of Gox1177 from Gluconobacter oxidans.
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
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Y B Yang et al.
Bioscience, biotechnology, and biochemistry, 56(9), 1392-1395 (1992-09-01)
The D-aminoacylase produced by Alcaligenes denitrificans DA181 was a new type of aminoacylase which had both high stereospecificity and specific activity. The molecular weight and isoelectric point of this enzyme were 58,000 and 4.4, respectively. The apparent Km and kcat
M Moriguchi et al.
Bioscience, biotechnology, and biochemistry, 57(7), 1149-1152 (1993-07-01)
The best inducers for D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 (Alcaligenes A-6) were a poor substrate, N-acetyl-gamma-methyl-D-leucine, and an inhibitor, N-acetyl-D-alloisoleucine. The enzyme has been homogeneously purified. The molecular weight of the native enzyme was estimated to be 58,000
Jennifer A Cummings et al.
Biochemistry, 48(27), 6469-6481 (2009-06-13)
The catalytic activities of three members of the amidohydrolase superfamily were discovered using amino acid substrate libraries. Bb3285 from Bordetella bronchiseptica, Gox1177 from Gluconobacter oxidans, and Sco4986 from Streptomyces coelicolor are currently annotated as d-aminoacylases or N-acetyl-d-glutamate deacetylases. These three
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